scholarly journals Eggshell membrane promotes homeostasis of elastic skin and lung tissue associated with type III collagen and decorin expression and ameliorates pulmonary fibrosis in a bleomycin mouse model

2021 ◽  
Author(s):  
Eri Ohto-Fujita ◽  
Miho Shimizu ◽  
Aya Atomi ◽  
Nozomi Hatakeyama ◽  
Shinya Horinouchi ◽  
...  
Keyword(s):  
Pulmonary Fibrosis ◽  
Mouse Model ◽  
Mouse Skin ◽  
Dermal Fibroblasts ◽  
Eggshell Membrane ◽  
Lung Fibroblasts ◽  
Papillary Dermis ◽  
Type Iii Collagen ◽  
Double Blind Study ◽  
Type Iii

Abstract The skin and lungs are barriers to environmental threats such as toxic chemicals and microbial pathogens. The integrity of the extracellular matrix (ECM) in the dermal papillae in the skin and the interstitium in the lungs is critical for tissue homeostasis. However, it is difficult to improve the ECM integrity in the skin and lung simultaneously. Previously, we reported that eggshell membrane (ESM) provided a young ECM environment to dermal fibroblasts in vitro and in mouse skin and increased the elasticity of human skin. Herein, lung fibroblasts cultured on ESM showed markedly higher type III collagen, decorin, and MMP2 levels. Oral ESM administration in mice markedly increased the type III collagen and decorin levels in lung tissues after 2 weeks, and type III collagen, decorin, and MMP2 levels in the papillary dermis after 4 weeks. Furthermore, in a double-blind study involving 30 adults, the arm skin elasticity significantly increased after 8 weeks of ESM administration. Simultaneously, the Tiffeneau-Pinelli index, which is correlated with lung elasticity, increased also significantly. To further explore the effects of ESM on the lungs, we used a mouse model of bleomycin-induced fibrosis. In these mice, ESM significantly suppressed fibrosis at 2 weeks and increased the type III collagen levels in the bronchioles and decorin levels in the alveoli, which was implicated in the suppression of lung fibrosis. Thus, oral ESM intake may prevent the age-dependent decline of the papillary dermis and pulmonary fibrosis by improving the extracellular environment in skin and lung tissues.

scholarly journals Eggshell membrane promotes homeostasis of elastic skin and lung tissue associated with type III collagen and decorin expression and ameliorates pulmonary fibrosis in a bleomycin mouse model

2021 ◽  
Author(s):  
Eri Ohto-Fujita ◽  
Miho Shimizu ◽  
Aya Atomi ◽  
Nozomi Hatakeyama ◽  
Shinya Horinouchi ◽  
...  
Keyword(s):  
Pulmonary Fibrosis ◽  
Mouse Model ◽  
Mouse Skin ◽  
Dermal Fibroblasts ◽  
Eggshell Membrane ◽  
Lung Fibroblasts ◽  
Papillary Dermis ◽  
Type Iii Collagen ◽  
Double Blind Study ◽  
Type Iii

Abstract The skin and lungs are barriers to environmental threats such as toxic chemicals and microbial pathogens. The integrity of the extracellular matrix (ECM) in the dermal papillae in the skin and the interstitium in the lungs is critical for tissue homeostasis. However, it is difficult to improve the ECM integrity in the skin and lung simultaneously. Previously, we reported that eggshell membrane (ESM) provided a young ECM environment to dermal fibroblasts in vitro and in mouse skin and increased the elasticity of human skin. Herein, lung fibroblasts cultured on ESM showed markedly higher type III collagen, decorin, and MMP2 levels. Oral ESM administration in mice markedly increased the type III collagen and decorin levels in lung tissues after 2 weeks, and type III collagen, decorin, and MMP2 levels in the papillary dermis after 4 weeks. Furthermore, in a double-blind study involving 30 adults, the arm skin elasticity significantly increased after 8 weeks of ESM administration. Simultaneously, the Tiffeneau-Pinelli index, which is correlated with lung elasticity, increased also significantly. To further explore the effects of ESM on the lungs, we used a mouse model of bleomycin-induced fibrosis. In these mice, ESM significantly suppressed fibrosis at 2 weeks and increased the type III collagen levels in the bronchioles and decorin levels in the alveoli, which was implicated in the suppression of lung fibrosis. Thus, oral ESM intake may prevent the age-dependent decline of the papillary dermis and pulmonary fibrosis by improving the extracellular environment in skin and lung tissues.

scholarly journals POS0431 FIBROBLASTS ARE NOT JUST FIBROBLASTS - CLEAR DIFFERENCES IN ECM PRODUCTION BETWEEN DERMAL AND LUNG FIBROBLASTS IN RESPONSE TO GROWTH FACTORS

2021 ◽  
Vol 80 (Suppl 1) ◽  
pp. 444.1-444
Author(s):  
S. F. Madsen ◽  
A. S. Siebuhr ◽  
H. Jessen ◽  
J. M. B. Sand ◽  
M. Karsdal ◽  
...  
Keyword(s):  
Lung Fibrosis ◽  
Treatment Initiation ◽  
Dermal Fibroblasts ◽  
Lung Fibroblasts ◽  
Type Iii Collagen ◽  
Type I ◽  
Migration Activity ◽  
Collagen Formation ◽  
Type Iii ◽  
Tgf Β1

Background:Many systemic sclerosis (SSc) patients develop lung fibrosis, which contribute significantly to increased mortality1. Activated and proliferating fibroblasts are responsible for the excessive extracellular matrix (ECM) formation and stiffening of the connective tissue leading to skin and lung fibrosis. There is currently no effective treatment for the fibrosis in SSc and there is therefore a medical need for further understanding the pathogenesis of fibrosis. Fibrosis is associated with different growth factors, including tumor growth factor beta 1 (TGF-β1) and platelet derived growth factor-ab (PDGF-ab)2.Objectives:We investigated how stimulation with TGF-β1 and PDGF-ab affected the migration capacity and the ECM production using translational biomarkers of type I, III and VI collagens in healthy human dermal and lung fibroblasts.Methods:The fibroblasts were grown in DMEM media containing 0.4% fetal calf serum, ficoll (to produce a crowded environment) and ascorbic acid for up to 12 days. The cells were stimulated with TGF-β1 [0.04-1 nM] or PDGF-ab [3 nM] at treatment initiation and changed twice a week. Non-stimulated fibroblasts (w/o) were used as control. A wound was induced by scratching the cells at day 1 after treatment initiation and the migration was followed for 2 days. Type I, III and VI collagen formation (PRO-C1, PRO-C3 and PRO-C6, respectively) were evaluated by validated ELISAs (Nordic Bioscience) in supernatant from day 0, 4, 8 and 12. Statistical analysis included 2-way ANOVA and Dunnett’s test.Results:The PDGF-ab stimulated dermal fibroblasts migrated significantly more than the non-stimulated (p<0.0001) and TGF-β1 stimulated (p<0.001) dermal fibroblasts 48 hours after the scratch (migration app. 70%, 30% and 30% respectively). There was no difference between the migration of the non-stimulated, TGF-β1 and PDGF-ab stimulated lung fibroblasts after 48 hours, as all migrated to approximately 70%.TGF-β1 stimulation led to a significant increase in type I collagen formation (PRO-C1) in both dermal and lung fibroblasts from day 4 and onwards compared to w/o (p<0.0001). TGF-β1 also lead to a significant increase in type III collagen formation (PRO-C3) from day 8 in lung fibroblasts compared to w/o (p<0.0001). PDGF-ab stimulation led to a significant increase in type III collagen formation in dermal fibroblasts from day 8 compared to w/o (p<0.0001). PDGF-ab stimulation led to a significant increase in type VI collagen formation (PRO-C6) in both dermal and lung fibroblasts from day 4 and onwards compared to w/o (p<0.0001).Conclusion:PDGF-ab increased the migration activity of the dermal fibroblasts, where the lung fibroblasts had a general high migration activity. The dermal and lung fibroblasts showcase the same ECM production within both type I and type VI collagen formation. The two fibroblasts types did however react opposite each other regarding the type III collagen formation: the dermal fibroblasts responded to PDGF-ab stimulation, where the lung fibroblasts responded to the TGF-β1 stimulation. The clear differences in the ECM production between the dermal and lung fibroblasts can be important in the search for an effective treatment for fibrosis in SSc and related lung fibrosis.References:[1]McNearney, T. A. et al. Pulmonary involvement in systemic sclerosis: Associations with genetic, serologic, sociodemographic, and behavioral factors. Arthritis Care Res.57, 318–326 (2007).[2]Wynn, T. A. Common and unique mechanisms regulate fibrosis in various fibroproliferative diseases. J. Clin. Invest.117, 524–529 (2007).Disclosure of Interests:Sofie Falkenløve Madsen Employee of: Nordic Bioscience and University of Copenhagen, Anne Sofie Siebuhr Employee of: Nordic Bioscience A/S, Henrik Jessen: None declared, Jannie Marie Bülow Sand Employee of: Nordic Bioscience A/S, Morten Karsdal Shareholder of: Nordic Bioscience A/S, Employee of: Nordic Bioscience A/S, Anne-Christine Bay-Jensen Shareholder of: Nordic Bioscience A/S, Employee of: Nordic Bioscience A/S

scholarly journals Subpopulations of rat lung fibroblasts with different amounts of type I and type III collagen mRNAs.

1990 ◽  
Vol 265 (11) ◽  
pp. 6286-6290
Author(s):  
E Breen ◽  
V M Falco ◽  
M Absher ◽  
K R Cutroneo
Keyword(s):  
Lung Fibroblasts ◽  
Type Iii Collagen ◽  
Type I ◽  
Rat Lung ◽  
Type Iii

scholarly journals Solubilized eggshell membrane supplies a type III collagen-rich elastic dermal papilla

2018 ◽  
Vol 376 (1) ◽  
pp. 123-135 ◽  
Author(s):  
Eri Ohto-Fujita ◽  
Miho Shimizu ◽  
Shoei Sano ◽  
Masashi Kurimoto ◽  
Kai Yamazawa ◽  
...  
Keyword(s):  
Dermal Papilla ◽  
Eggshell Membrane ◽  
Type Iii Collagen ◽  
Type Iii

scholarly journals Asiaticoside induces cell proliferation and collagen synthesis in human dermal fibroblasts

2015 ◽  
Vol 34 (2) ◽  
pp. 96
Author(s):  
Linda Yuliati ◽  
Etik Mardliyati ◽  
Kusmarinah Bramono ◽  
Hans Joachim Freisleben
Keyword(s):  
Cell Proliferation ◽  
Wound Healing ◽  
Retinoic Acid ◽  
Collagen Synthesis ◽  
Active Agent ◽  
Dermal Fibroblasts ◽  
Type Iii Collagen ◽  
Type I ◽  
Human Dermal Fibroblasts ◽  
Type Iii

Background<br />Asiatiocoside, a saponin component isolated from Centella asiatica can improve wound healing by promoting the proliferation of human dermal fibroblasts (HDF) and synthesis of collagen. The skin-renewing cells and type I and III collagen synthesis decrease with aging, resulting in the reduction of skin elasticity and delayed wound healing. Usage of natural active compounds from plants in wound healing should be evaluated and compared to retinoic acid as an active agent that regulates wound healing. The aim of this study was to compare and evaluate the effect of asiaticoside and retinoic acid to induce greater cell proliferation and type I and III collagen synthesis in human dermal fibroblast.<br /><br />Methods<br />Laboratory experiments were conducted using human dermal fibroblasts (HDF) isolated from human foreskin explants. Seven passages of HDF were treated with asiaticoside and retinoic acid at several doses and incubated for 24 and 48 hours. Cell viability in all groups was tested with the MTT assay to assess HDF proliferation. Type I and III collagen synthesis was examined using the respective ELISA kits. Analysis of variance was performed to compare the treatment groups. <br /><br />Results<br />Asiaticoside had significantly stronger effects on HDF proliferation than retinoic acid (p&lt;0.05). The type III collagen production was significantly greater induction with asiaticoside compared to retinoic acid (p&lt;0.05). <br /><br />Conclusion<br />Asiaticoside induces HDF proliferation and type I and III collagen synthesis in a time- and dose-dependent pattern. Asiaticoside has a similar effect as retinoic acid on type I and type III collagen synthesis.

scholarly journals Retraction Note to: Coexpression of HSP47 Gene and Type I and Type III Collagen Genes in LPS-Induced Pulmonary Fibrosis in Rats

Lung ◽  
2015 ◽  
Vol 193 (4) ◽  
pp. 617-617
Author(s):  
Satoshi Hagiwara ◽  
Hideo Iwasaka ◽  
Shigekiyo Matsumoto ◽  
Takayuki Noguchi ◽  
Hidekatsu Yoshioka
Keyword(s):  
Pulmonary Fibrosis ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Collagen Genes

Type III collagen affects dermal and vascular collagen fibrillogenesis and tissue integrity in a mutant Col3a1 transgenic mouse model

2018 ◽  
Vol 70 ◽  
pp. 72-83 ◽  
Author(s):  
Sanne D'hondt ◽  
Brecht Guillemyn ◽  
Delfien Syx ◽  
Sofie Symoens ◽  
Riet De Rycke ◽  
...  
Keyword(s):  
Mouse Model ◽  
Transgenic Mouse ◽  
Transgenic Mouse Model ◽  
Type Iii Collagen ◽  
Collagen Fibrillogenesis ◽  
Type Iii ◽  
Tissue Integrity

scholarly journals Galectin-3 levels are elevated following nintedanib treatment

2020 ◽  
Vol 11 ◽  
pp. 204062232096841
Author(s):  
Gali Epstein Shochet ◽  
Alon Pomerantz ◽  
David Shitrit ◽  
Becky Bardenstein-Wald ◽  
Kjetil Ask ◽  
...  
Keyword(s):  
Pulmonary Fibrosis ◽  
Mouse Model ◽  
Quantitative Polymerase Chain Reaction ◽  
Lung Fibroblasts ◽  
Mrna Levels ◽  
Serum Samples ◽  
In Vivo Models ◽  
Galectin 3 ◽  
The Impact

Background and Aims: Idiopathic pulmonary fibrosis (IPF) is a common and severe form of pulmonary fibrosis. Nintedanib, a triple angiokinase inhibitor, is approved for treating IPF. Galectin 3 (Gal-3) activates a variety of profibrotic processes. Currently, the Gal-3 inhibitor TD139 is being tested in phase II clinical trials. Since this treatment is given ‘on top’ of nintedanib, it is important to estimate its effect on Gal-3 levels. Therefore, we evaluated the impact of nintedanib on Gal-3 expression using both in vitro and in vivo models, in addition to serum samples from patients with IPF. Methods: Gal-3 levels were evaluated in IPF and control tissue samples, primary human lung fibroblasts (HLFs) following nintedanib treatment (10–100 nM, quantitative polymerase chain reaction), and in a silica-induced fibrosis mouse model with/without nintedanib (0.021–0.21 mg/kg) by immunohistochemistry. In addition, Gal-3 levels were analyzed in serum samples from 41 patients with interstitial lung disease patients with/without nintedanib treatment by ELISA. Results: Nintedanib addition to HLFs resulted in significant elevations in Gal-3, phospho-signal transducer and activator of transcription 3 (pSTAT3), as well as IL-8 mRNA levels ( p < 0.05). Gal-3 expression was higher in samples from IPF patients compared with non-IPF controls at the protein and mRNA levels ( p < 0.05). In the in vivo mouse model, Gal-3 levels were increased following fibrosis induction and even further increased with the addition of nintedanib, mostly in macrophages ( p < 0.05). Patients receiving nintedanib presented with higher Gal-3 serum levels compared with those who did not receive nintedanib ( p < 0.05). Conclusion: Nintedanib elevates Gal-3 levels in both experimental models, along with patient samples. These findings highlight the possibility of using combined inhibition therapy for patients with IPF.

scholarly journals Cosmetic Potential of a Recombinant 50 kDa Protein

Cosmetics ◽  
2022 ◽  
Vol 9 (1) ◽  
pp. 8
Author(s):  
Nesma Aly ◽  
Emilie Benoit ◽  
Jean-Luc Chaubard ◽  
Kavyasree Chintalapudi ◽  
Soojin Choung ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Collagen Type ◽  
Collagen Type I ◽  
Protein Product ◽  
Dermal Fibroblasts ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Extraction And Purification ◽  
Recombinant Type

Collagen and its derivative proteins have been widely used as a major component for cosmetic formulations as a natural ingredient and moisturizer. Most commercially available collagens are animal-derived collagen type I and other forms of collagen, such as type III collagen, are far less prevalent in animals, making extraction and purification extremely difficult and expensive. Here, we report the production of a 50 kDa protein produced in yeast that is 100% identical to the N-terminus of the human type III collagen. This recombinant protein has a larger molecular weight than most incumbent recombinant collagen proteins available for personal care applications. We report the industrialization of both the fermentation and purification processes to produce a final recombinant protein product. This final protein product was shown to be safe for general applications to human skin and compatible with common formulation protocols, including ethanol-based formulations. This recombinant collagen type III protein was also shown to uniquely stimulate both collagen type I and type III production and secretion by primary human dermal fibroblasts. The unique combination of biostimulation, compatibility with beauty product formulations and demonstrated commercial production, make this novel recombinant type III collagen a good candidate for broad application in the cosmetics industry.

Type I and Type III collagen mRNA expression in human lung fibroblasts

1994 ◽  
Vol 22 (1) ◽  
pp. 51S-51S ◽  
Author(s):  
MARIA C. MAGUIRE ◽  
CLARE M. O'CONNOR ◽  
MUIRIS X. FITZGERALD
Keyword(s):  
Mrna Expression ◽  
Human Lung ◽  
Lung Fibroblasts ◽  
Type Iii Collagen ◽  
Type I ◽  
Human Lung Fibroblasts ◽  
Type Iii ◽  
Collagen Mrna
Sign in / Sign up

Export Citation Format

Share Document